ID BCHB_RHOCB Reviewed; 525 AA. AC P26163; D5ANS5; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 25-JAN-2012, entry version 73. DE RecName: Full=Light-independent protochlorophyllide reductase subunit B; DE Short=DPOR subunit B; DE Short=LI-POR subunit B; DE EC=1.18.-.-; GN Name=bchB; Synonyms=bchK; OrderedLocusNames=RCAP_rcc00664; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX MEDLINE=93224465; PubMed=8385667; RA Burke D.H., Alberti M., Hearst J.E.; RT "bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus RT and identification of the third subunit of light-independent RT protochlorophyllide reductase in bacteria and plants."; RL J. Bacteriol. 175:2414-2422(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). RN [3] RP PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION. RC STRAIN=SB1003 / CB1029; RX MEDLINE=20378986; PubMed=10811655; DOI=10.1074/jbc.M002904200; RA Fujita Y., Bauer C.E.; RT "Reconstitution of light-independent protochlorophyllide reductase RT from purified bchL and bchN-bchB subunits. In vitro confirmation of RT nitrogenase-like features of a bacteriochlorophyll biosynthesis RT enzyme."; RL J. Biol. Chem. 275:23583-23588(2000). RN [4] RP CHARACTERIZATION. RA Fujita Y.; RL Unpublished observations (JUL-2001). CC -!- FUNCTION: Uses Mg-ATP and reduced ferredoxin to reduce ring D of CC protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). CC The BchN-BchB pair binds Pchlide. This reaction is light- CC independent. CC -!- PATHWAY: Porphyrin biosynthesis; bacteriochlorophyll biosynthesis CC (light-independent). CC -!- SUBUNIT: Protochlorophyllide reductase is thought to be composed CC of three subunits; BchL, BchN and BchB. Could form a CC heterotetramer of two BchB and two BchN subunits. CC -!- SIMILARITY: Belongs to the ChlB/BchB/BchZ family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11165; CAA77525.1; -; Genomic_DNA. DR EMBL; CP001312; ADE84429.1; -; Genomic_DNA. DR PIR; C49851; C49851. DR RefSeq; YP_003576836.1; NC_014034.1. DR PDB; 3AEK; X-ray; 2.30 A; B/D=1-525. DR PDB; 3AEQ; X-ray; 2.90 A; B/D=1-525. DR PDB; 3AER; X-ray; 2.80 A; B/D=1-525. DR PDB; 3AES; X-ray; 2.50 A; B/D=1-525. DR PDB; 3AET; X-ray; 2.91 A; B/D=1-525. DR PDB; 3AEU; X-ray; 2.90 A; B/D=1-525. DR PDBsum; 3AEK; -. DR PDBsum; 3AEQ; -. DR PDBsum; 3AER; -. DR PDBsum; 3AES; -. DR PDBsum; 3AET; -. DR PDBsum; 3AEU; -. DR ProteinModelPortal; P26163; -. DR GeneID; 9003493; -. DR KEGG; rcp:RCAP_rcc00664; -. DR PATRIC; 35501396; VBIRhoCap134200_0675. DR BioCyc; MetaCyc:MONOMER-13270; -. DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro. DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro. DR HAMAP; MF_00353; ChlB_BchB; 1; -. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR InterPro; IPR013580; P-CP/CP_red_C. DR InterPro; IPR005969; Protochl_reductB. DR InterPro; IPR016209; Protochlorophyllide_Rdtase. DR KO; K04039; -. DR Pfam; PF00148; Oxidored_nitro; 1. DR Pfam; PF08369; PCP_red; 1. DR PIRSF; PIRSF000163; PCP_ChlB; 1. DR TIGRFAMs; TIGR01278; DPOR_BchB; 1. PE 1: Evidence at protein level; KW 3D-structure; Bacteriochlorophyll biosynthesis; KW Chlorophyll biosynthesis; Complete proteome; KW Direct protein sequencing; Oxidoreductase; Photosynthesis. FT CHAIN 1 525 Light-independent protochlorophyllide FT reductase subunit B. FT /FTId=PRO_0000219800. FT HELIX 17 20 FT STRAND 23 31 FT HELIX 37 39 FT HELIX 40 45 FT STRAND 54 57 FT HELIX 62 64 FT HELIX 68 84 FT STRAND 87 93 FT HELIX 97 99 FT HELIX 108 111 FT STRAND 117 119 FT TURN 124 126 FT HELIX 134 144 FT STRAND 155 159 FT HELIX 168 180 FT STRAND 185 189 FT HELIX 196 200 FT STRAND 206 210 FT HELIX 218 226 FT HELIX 242 252 FT HELIX 266 271 FT HELIX 273 278 FT STRAND 282 285 FT HELIX 291 301 FT HELIX 315 317 FT HELIX 318 327 FT HELIX 338 348 FT STRAND 351 354 FT HELIX 357 365 FT STRAND 374 376 FT HELIX 379 381 FT HELIX 396 403 FT HELIX 411 417 SQ SEQUENCE 525 AA; 57192 MW; 4322A6D9F535C3F5 CRC64; MKLTLWTYEG PPHVGAMRVA TAMKDLQLVL HGPQGDTYAD LLFTMIERRN ARPPVSFSTF EASHMGTDTA ILLKDALAAA HARYKPQAMA VALTCTAELL QDDPNGISRA LNLPVPVVPL ELPSYSRKEN YGADETFRAL VRALAVPMER TPEVTCNLLG ATALGFRHRD DVAEVTKLLA TMGIKVNVCA PLGASPDDLR KLGQAHFNVL MYPETGESAA RHLERACKQP FTKIVPIGVG ATRDFLAEVS KITGLPVVTD ESTLRQPWWS ASVDSTYLTG KRVFIFGDGT HVIAAARIAA KEVGFEVVGM GCYNREMARP LRTAAAEYGL EALITDDYLE VEKAIEAAAP ELILGTQMER NIAKKLGLPC AVISAPVHVQ DFPARYAPQM GFEGANVLFD TWVHPLVMGL EEHLLTMFRE DFEFHDAAGA SHHGGKAVAR EESPVAPADL APAATSDTPA APSPVVVTQA SGEIRWMPEA ERELRKIPFF VRGKAKRNTE LYAAHKGVCD ITVETLYEAK AHYAR //